Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0HYW0 (ALR_SHESR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine racemase

EC=5.1.1.1
Gene names
Name:alr
Ordered Locus Names:Shewmr7_0693
OrganismShewanella sp. (strain MR-7) [Complete proteome] [HAMAP]
Taxonomic identifier60481 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids By similarity. HAMAP-Rule MF_01201

Catalytic activity

L-alanine = D-alanine. HAMAP-Rule MF_01201

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01201

Pathway

Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. HAMAP-Rule MF_01201

Sequence similarities

Belongs to the alanine racemase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionalanine racemase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Alanine racemase HAMAP-Rule MF_01201
PRO_1000164623

Sites

Active site351Proton acceptor; specific for D-alanine By similarity
Active site2551Proton acceptor; specific for L-alanine By similarity
Binding site1301Substrate By similarity
Binding site3031Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0HYW0 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 98DEDEAA7075EA9C

FASTA35838,667
        10         20         30         40         50         60 
MKPFPRAEIS SSALQNNLAV LRQQASRSQV MAVVKANGYG HGLLNVANCL HTADGFGLAR 

        70         80         90        100        110        120 
LEEALELRAG GVKARLLLLE GFFRSTDLPL LVAHDIDTVV HHESQIEMLE QATLSKPVTV 

       130        140        150        160        170        180 
WLKVDSGMHR LGVTPEQFAQ VYARLTACDN VAKPIHLMTH FACADEPENN YTQVQMQTFN 

       190        200        210        220        230        240 
QLTADLPGFR TLANSAGALY WPKSQGDWIR PGIALYGVSP VTGDCGANHG LIPAMNLVSR 

       250        260        270        280        290        300 
LIAVRDHKAG QPVGYGCYWT AKQDTRLGVV AIGYGDGYPR NAPEGTPVWV NGRRVPIVGR 

       310        320        330        340        350 
VSMDMLTVDL GADAADQVGD EALLWGAALP VEEVAEHIGT IAYELVTKLT PRVAVCLA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Shewanella sp. MR-7."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MR-7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000444 Genomic DNA. Translation: ABI41695.1.
RefSeqYP_736752.1. NC_008322.1.

3D structure databases

ProteinModelPortalQ0HYW0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING60481.Shewmr7_0693.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI41695; ABI41695; Shewmr7_0693.
GeneID4256871.
KEGGshm:Shewmr7_0693.
PATRIC23586289. VBISheSp85603_0722.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0787.
HOGENOMHOG000031446.
KOK01775.
OMAINNQLAP.
OrthoDBEOG6PP9NJ.
ProtClustDBPRK00053.

Enzyme and pathway databases

BioCycSSP60481:GHW6-722-MONOMER.
UniPathwayUPA00042; UER00497.

Family and domain databases

Gene3D2.40.37.10. 1 hit.
HAMAPMF_01201. Ala_racemase.
InterProIPR000821. Ala_racemase.
IPR009006. Ala_racemase/Decarboxylase_C.
IPR011079. Ala_racemase_C.
IPR001608. Ala_racemase_N.
IPR020622. Ala_racemase_pyridoxalP-BS.
[Graphical view]
PfamPF00842. Ala_racemase_C. 1 hit.
PF01168. Ala_racemase_N. 1 hit.
[Graphical view]
PRINTSPR00992. ALARACEMASE.
SMARTSM01005. Ala_racemase_C. 1 hit.
[Graphical view]
SUPFAMSSF50621. SSF50621. 1 hit.
TIGRFAMsTIGR00492. alr. 1 hit.
PROSITEPS00395. ALANINE_RACEMASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALR_SHESR
AccessionPrimary (citable) accession number: Q0HYW0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways